Specificity of lectin activity ofBacillus thuringiensis parasporal inclusion proteins

Akao, Tetsuyuki; Mizuki, Eiichi; Yamashita, Satoko; Kim, Ho-San; Lee, Dae-Weon; Ohba, Michio

doi:10.1002/1521-4028(200103)41:1<3::aid-jobm3>3.0.co;2-e

Cited by 3 publications

(1 citation statement)

References 11 publications

(8 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A decade later, Berliner isolated a Gram-positive bacterium in Ephesitia kuehniella larvae in the state of Thuringia (Germany). Ignoring the identification given by Ishiwata, Berliner designated the bacterium as Bacillus thuringiensis, and this nomenclature has remained ever since [3].…”

Section: Introductionmentioning

confidence: 99%

Genetic Modification Approaches for Parasporins Bacillus thuringiensis Proteins with Anticancer Activity

et al. 2021

View full text Add to dashboard Cite

Bacillus thuringiensis (Bt) is a bacterium capable of producing Cry toxins, which are recognized for their bio-controlling actions against insects. However, a few Bt strains encode proteins lacking insecticidal activity but showing cytotoxic activity against different cancer cell lines and low or no cytotoxicity toward normal human cells. A subset of Cry anticancer proteins, termed parasporins (PSs), has recently arisen as a potential alternative for cancer treatment. However, the molecular receptors that allow the binding of PSs to cells and their cytotoxic mechanisms of action have not been well established. Nonetheless, their selective cytotoxic activity against different types of cancer cell lines places PSs as a promising alternative treatment modality. In this review, we provide an overview of the classification, structures, mechanisms of action, and insights obtained from genetic modification approaches for PS proteins.

show abstract

Section: Introductionmentioning

confidence: 99%

Genetic Modification Approaches for Parasporins Bacillus thuringiensis Proteins with Anticancer Activity

et al. 2021

View full text Add to dashboard Cite

show abstract

Mannose-Specific Lectin Activity of Parasporal Proteins from a Lepidoptera-Specific Bacillus thuringiensis Strain

Wasano

Ohgushi

Ohba

2003

Current Microbiology

View full text Add to dashboard Cite

Lectin activity, agglutinating sheep erythrocytes, was associated with parasporal inclusion proteins from a Lepidoptera-specific isolate of Bacillus thuringiensis serovar galleriae (H5ab). The activity was generated when parasporal inclusions were solubilized in an alkaline condition. Proteolytic processing was not required for generation of the lectin activity; the activity level was not affected by the presence/absence of the three proteases (trypsin, chymotrypsin, and proteinase K). SDS-PAGE analysis revealed that (1) alkali-solubilized parasporal inclusion proteins consisted of two major components of 130 kDa and 65 kDa, and (2) proteinase K treatment of alkali-solubilized proteins yielded a single major protein of 60 kDa. Lectin activity of our isolate was strongly inhibited by preincubation with D-mannose, but not with the six other monosaccharides: D-galactose, D-glucose, L-fucose, N-acetyl- D-glucosamine, N-acetyl- D-galactosamine, and N-acetylneuraminic acid. In contrast, D-mannose did not inhibit the in vivo larvicidal activity of the proteins against the silkworm, Bombyx mori.

show abstract

Characterization of Flagellar Antigens and Insecticidal Activities of Bacillus thuringiensis Populations in Animal Feces

Lee

Shisa

Wasano

et al. 2003

Current Microbiology

View full text Add to dashboard Cite

In total, 287 Bacillus thuringiensis isolates, recovered from feces of 28 zoo-maintained animal species, were examined for flagellar (H) antigenicity and insecticidal activity. Serologically, 209 isolates (72.8%) were allocated to the 8 H serogroups, 4 were untypable, and 74 were untestable. Among the 8 H serotypes detected, H3abc (serovar kurstaki) predominated at a high frequency of 88.0%, followed by H6 (serovar entomocidus) with a frequency of 7.7%. Insecticidal activity was associated with 67.2% of the fecal populations: 188 isolates were toxic to both Bombyx mori (Lepidoptera: Bombycidae) and Aedes aegypti (Diptera: Culicidae), 2 isolates were specific for B. mori, and 3 isolates were toxic to A. aegypti only. Of the isolates with dual toxicity, 97.9% belonged to the serovar kurstaki, producing bipyramidal parasporal inclusions. All of the H7 (serovar aizawai) isolates were toxic to both insects.

show abstract

Specificity of lectin activity ofBacillus thuringiensis parasporal inclusion proteins

Cited by 3 publications

References 11 publications

Genetic Modification Approaches for Parasporins Bacillus thuringiensis Proteins with Anticancer Activity

Genetic Modification Approaches for Parasporins Bacillus thuringiensis Proteins with Anticancer Activity

Mannose-Specific Lectin Activity of Parasporal Proteins from a Lepidoptera-Specific Bacillus thuringiensis Strain

Characterization of Flagellar Antigens and Insecticidal Activities of Bacillus thuringiensis Populations in Animal Feces

Contact Info

Product

Resources

About